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DNA targets for certain bZIP proteins distinguished by an intrinsic bend
D N Paolella1, C R Palmer, A Schepartz
1Department of Chemistry, Yale University, New Haven, CT 06511.
Science (New York, N.Y.)
|May 20, 1994
Summary
Basic region leucine zipper (bZIP) proteins show sequence conservation but differ in DNA target binding. Their half-site spacing preferences arise from DNA target site curvature and bZIP protein adaptability.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Basic region leucine zipper (bZIP) proteins are transcription factors with conserved DNA-binding segments.
- Despite sequence conservation, bZIP proteins exhibit varying preferences for target DNA half-site spacing.
Purpose of the Study:
- To investigate the molecular mechanisms underlying the differential half-site spacing preferences of bZIP proteins.
- To elucidate how bZIP proteins discriminate between DNA target sequences with variations in spacing.
Main Methods:
- Analysis of DNA target site intrinsic curvature.
- Investigation of bZIP protein binding mechanisms.
- Examination of basic segment residue roles in overcoming DNA curvature.
Main Results:
- Differential intrinsic curvature in target binding sites with single base pair insertions or deletions influences bZIP protein binding.
- Some bZIP proteins can overcome this intrinsic DNA curvature.
- This overcoming mechanism is dependent on specific residues within the basic segment of the bZIP proteins.
Conclusions:
- bZIP protein half-site spacing preferences are determined by both DNA target site properties and protein adaptability.
- The ability of certain bZIP proteins to adapt to DNA curvature is crucial for their specific target recognition.